CATB_MOUSE
ID CATB_MOUSE Reviewed; 339 AA.
AC P10605; Q3UDW7;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Cathepsin B;
DE EC=3.4.22.1 {ECO:0000250|UniProtKB:P07858};
DE AltName: Full=Cathepsin B1;
DE Contains:
DE RecName: Full=Cathepsin B light chain {ECO:0000250|UniProtKB:P07858};
DE Contains:
DE RecName: Full=Cathepsin B heavy chain {ECO:0000250|UniProtKB:P07858};
DE Flags: Precursor;
GN Name=Ctsb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=2012677; DOI=10.1089/dna.1991.10.159;
RA Qian F., Frankfater A., Chan S.J., Steiner D.F.;
RT "The structure of the mouse cathepsin B gene and its putative promoter.";
RL DNA Cell Biol. 10:159-168(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=2226854; DOI=10.1016/0014-5793(90)81083-z;
RA Ferrara M., Wojcik F., Rhaissi H., Mordier S., Roux M.-P., Bechet D.;
RT "Gene structure of mouse cathepsin B.";
RL FEBS Lett. 273:195-199(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3463996; DOI=10.1073/pnas.83.20.7721;
RA Chan S.J., San Segundo B., McCormick M.B., Steiner D.F.;
RT "Nucleotide and predicted amino acid sequences of cloned human and mouse
RT preprocathepsin B cDNAs.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:7721-7725(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=1746902;
RA Qian F., Frankfater A., Steiner D.F., Bajkowski A.S., Chan S.J.;
RT "Characterization of multiple cathepsin B mRNAs in murine B16a melanoma.";
RL Anticancer Res. 11:1445-1451(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Placenta, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 314-339.
RX PubMed=1889751; DOI=10.1016/0378-1119(91)90283-h;
RA Friemert C., Closs E.I., Silbermann M., Erfle V., Strauss P.G.;
RT "Isolation of a cathepsin B-encoding cDNA from murine osteogenic cells.";
RL Gene 103:259-261(1991).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=12782676; DOI=10.1172/jci200315990;
RA Friedrichs B., Tepel C., Reinheckel T., Deussing J., von Figura K.,
RA Herzog V., Peters C., Saftig P., Brix K.;
RT "Thyroid functions of mouse cathepsins B, K, and L.";
RL J. Clin. Invest. 111:1733-1745(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-220, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Thiol protease which is believed to participate in
CC intracellular degradation and turnover of proteins (By similarity).
CC Cleaves matrix extracellular phosphoglycoprotein MEPE (By similarity).
CC Involved in the solubilization of cross-linked TG/thyroglobulin in the
CC thyroid follicle lumen (PubMed:12782676). Has also been implicated in
CC tumor invasion and metastasis (By similarity).
CC {ECO:0000250|UniProtKB:P07858, ECO:0000269|PubMed:12782676}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with broad specificity for peptide
CC bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule
CC substrates (thus differing from cathepsin L). In addition to being an
CC endopeptidase, shows peptidyl-dipeptidase activity, liberating C-
CC terminal dipeptides.; EC=3.4.22.1;
CC Evidence={ECO:0000250|UniProtKB:P07858};
CC -!- SUBUNIT: Dimer of a heavy chain and a light chain cross-linked by a
CC disulfide bond. Interacts with SRPX2. Directly interacts with SHKBP1.
CC {ECO:0000250|UniProtKB:P07858}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:12782676}.
CC Melanosome {ECO:0000250|UniProtKB:P07858}. Secreted, extracellular
CC space {ECO:0000269|PubMed:12782676}. Apical cell membrane
CC {ECO:0000269|PubMed:12782676}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12782676}; Extracellular side
CC {ECO:0000269|PubMed:12782676}. Note=Localizes to the lumen of thyroid
CC follicles and to the apical membrane of thyroid epithelial cells.
CC {ECO:0000269|PubMed:12782676}.
CC -!- TISSUE SPECIFICITY: Expressed in thyroid epithelial cells.
CC {ECO:0000269|PubMed:12782676}.
CC -!- DISRUPTION PHENOTYPE: Enlarged thyroid follicles, reduced extension of
CC the thyroid epithelium, and increased levels of Tg/thyroglobulin in the
CC thyroid follicles which fails to assemble into multilayers. Lysosomes
CC are enlarged and CTSK/cathepsin K is absent from the thyroid follicle
CC lumen and mis-localizes to the apical membrane of thyroid epithelial
CC cells. {ECO:0000269|PubMed:12782676}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR EMBL; M65270; AAA37375.1; -; Genomic_DNA.
DR EMBL; M65263; AAA37375.1; JOINED; Genomic_DNA.
DR EMBL; M65264; AAA37375.1; JOINED; Genomic_DNA.
DR EMBL; M65265; AAA37375.1; JOINED; Genomic_DNA.
DR EMBL; M65266; AAA37375.1; JOINED; Genomic_DNA.
DR EMBL; M65267; AAA37375.1; JOINED; Genomic_DNA.
DR EMBL; M65268; AAA37375.1; JOINED; Genomic_DNA.
DR EMBL; M65269; AAA37375.1; JOINED; Genomic_DNA.
DR EMBL; M14222; AAA37494.1; -; mRNA.
DR EMBL; X54966; CAA38713.1; -; mRNA.
DR EMBL; S69034; AAB20536.1; -; mRNA.
DR EMBL; AK083393; BAC38900.1; -; mRNA.
DR EMBL; AK147192; BAE27751.1; -; mRNA.
DR EMBL; AK149884; BAE29144.1; -; mRNA.
DR EMBL; AK151790; BAE30691.1; -; mRNA.
DR EMBL; AK167361; BAE39458.1; -; mRNA.
DR EMBL; BC006656; AAH06656.1; -; mRNA.
DR CCDS; CCDS27197.1; -.
DR PIR; A38458; KHMSB.
DR RefSeq; NP_031824.1; NM_007798.3.
DR AlphaFoldDB; P10605; -.
DR SMR; P10605; -.
DR BioGRID; 198968; 19.
DR ComplexPortal; CPX-100; Cathepsin-B - cystatin-A complex.
DR IntAct; P10605; 9.
DR MINT; P10605; -.
DR STRING; 10090.ENSMUSP00000006235; -.
DR BindingDB; P10605; -.
DR ChEMBL; CHEMBL5187; -.
DR MEROPS; C01.060; -.
DR GlyConnect; 2189; 3 N-Linked glycans (1 site).
DR GlyGen; P10605; 1 site, 3 N-linked glycans (1 site).
DR iPTMnet; P10605; -.
DR PhosphoSitePlus; P10605; -.
DR SwissPalm; P10605; -.
DR SWISS-2DPAGE; P10605; -.
DR CPTAC; non-CPTAC-3564; -.
DR EPD; P10605; -.
DR jPOST; P10605; -.
DR MaxQB; P10605; -.
DR PaxDb; P10605; -.
DR PeptideAtlas; P10605; -.
DR PRIDE; P10605; -.
DR ProteomicsDB; 281221; -.
DR Antibodypedia; 4373; 684 antibodies from 42 providers.
DR DNASU; 13030; -.
DR Ensembl; ENSMUST00000006235; ENSMUSP00000006235; ENSMUSG00000021939.
DR GeneID; 13030; -.
DR KEGG; mmu:13030; -.
DR UCSC; uc007uhh.2; mouse.
DR CTD; 1508; -.
DR MGI; MGI:88561; Ctsb.
DR VEuPathDB; HostDB:ENSMUSG00000021939; -.
DR eggNOG; KOG1543; Eukaryota.
DR GeneTree; ENSGT00940000158680; -.
DR HOGENOM; CLU_012184_3_3_1; -.
DR InParanoid; P10605; -.
DR OMA; DEKIPYW; -.
DR OrthoDB; 865289at2759; -.
DR PhylomeDB; P10605; -.
DR TreeFam; TF314576; -.
DR BioCyc; MetaCyc:MON-14810; -.
DR BRENDA; 3.4.22.1; 3474.
DR BRENDA; 3.4.23.5; 3474.
DR Reactome; R-MMU-1442490; Collagen degradation.
DR Reactome; R-MMU-1679131; Trafficking and processing of endosomal TLR.
DR Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 13030; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Ctsb; mouse.
DR PRO; PR:P10605; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P10605; protein.
DR Bgee; ENSMUSG00000021939; Expressed in stroma of bone marrow and 276 other tissues.
DR Genevisible; P10605; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0005901; C:caveola; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:1904090; C:peptidase inhibitor complex; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; ISO:MGI.
DR GO; GO:0005518; F:collagen binding; ISO:MGI.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IDA:MGI.
DR GO; GO:0004175; F:endopeptidase activity; IMP:UniProtKB.
DR GO; GO:0030984; F:kininogen binding; ISO:MGI.
DR GO; GO:0008233; F:peptidase activity; ISO:MGI.
DR GO; GO:0042277; F:peptide binding; ISO:MGI.
DR GO; GO:0043621; F:protein self-association; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0043394; F:proteoglycan binding; ISO:MGI.
DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEA:Ensembl.
DR GO; GO:0030574; P:collagen catabolic process; ISO:MGI.
DR GO; GO:0046697; P:decidualization; IGI:MGI.
DR GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:0010466; P:negative regulation of peptidase activity; ISO:MGI.
DR GO; GO:0030163; P:protein catabolic process; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IMP:UniProtKB.
DR GO; GO:0006590; P:thyroid hormone generation; IMP:UniProtKB.
DR GO; GO:0046718; P:viral entry into host cell; IMP:CACAO.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR012599; Propeptide_C1A.
DR Pfam; PF00112; Peptidase_C1; 1.
DR Pfam; PF08127; Propeptide_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Disulfide bond; Glycoprotein; Hydrolase;
KW Lysosome; Membrane; Protease; Reference proteome; Secreted; Signal;
KW Thiol protease; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..79
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT /id="PRO_0000026148"
FT CHAIN 80..333
FT /note="Cathepsin B"
FT /id="PRO_0000026149"
FT CHAIN 80..126
FT /note="Cathepsin B light chain"
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT /id="PRO_0000026150"
FT CHAIN 129..333
FT /note="Cathepsin B heavy chain"
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT /id="PRO_0000026151"
FT PROPEP 334..339
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT /id="PRO_0000026152"
FT ACT_SITE 108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT ACT_SITE 278
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT ACT_SITE 298
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT MOD_RES 220
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT DISULFID 93..122
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT DISULFID 105..150
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT DISULFID 141..207
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT DISULFID 142..146
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT DISULFID 179..211
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT DISULFID 187..198
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT CONFLICT 160
FT /note="S -> N (in Ref. 3; AAA37494)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="N -> D (in Ref. 3; AAA37494)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="V -> I (in Ref. 3; AAA37494)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="G -> V (in Ref. 3; AAA37494)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 339 AA; 37280 MW; 9F0A3CDF70A94040 CRC64;
MWWSLILLSC LLALTSAHDK PSFHPLSDDL INYINKQNTT WQAGRNFYNV DISYLKKLCG
TVLGGPKLPG RVAFGEDIDL PETFDAREQW SNCPTIGQIR DQGSCGSCWA FGAVEAISDR
TCIHTNGRVN VEVSAEDLLT CCGIQCGDGC NGGYPSGAWS FWTKKGLVSG GVYNSHVGCL
PYTIPPCEHH VNGSRPPCTG EGDTPRCNKS CEAGYSPSYK EDKHFGYTSY SVSNSVKEIM
AEIYKNGPVE GAFTVFSDFL TYKSGVYKHE AGDMMGGHAI RILGWGVENG VPYWLAANSW
NLDWGDNGFF KILRGENHCG IESEIVAGIP RTDQYWGRF
